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Science 1 February 1991:
Vol. 251. no. 4993, pp. 558 - 560
DOI: 10.1126/science.1990431
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Articles

Science, Vol 251, Issue 4993, 558-560
Copyright © 1991 by American Association for the Advancement of Science

articles

Transducin activation by rhodopsin without a covalent bond to the 11-cis-retinal chromophore

EA Zhukovsky, PR Robinson, and DD Oprian

Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.

Rhodopsin and the visual pigments are a distinct group within the family of G-protein-linked receptors in that they have a covalently bound ligand, the 11-cis-retinal chromophore, whereas all of the other receptors bind their agonists through noncovalent interactions. The retinal chromophore in rhodopsin is bound by means of a protonated Schiff base linkage to the epsilon-amino group of Lys-296. Two rhodopsin mutants have been constructed, K296G and K296A, in which the covalent linkage to the chromophore is removed. Both mutants form a pigment with an absorption spectrum close to that of the wild type when reconstituted with the Schiff base of an n-alkylamine and 11-cis-retinal. In addition, the pigment formed from K296G and the n-propylamine Schiff base of 11-cis-retinal was found to activate transducin in a light-dependent manner, with 30 to 40% of the specific activity measured for the wild-type protein. It appears that the covalent bond is not essential for binding of the chromophore or for catalytic activation of transducin.


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